来自大肠杆菌的5-酮-4-脱氧uronate异构酶的结晶。
Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli.
作者信息
Dunten P, Jaffe H, Aksamit R R
机构信息
Department of Molecular Biology, Swedish University of Agricultural Sciences, BMC Box 590, Uppsala 75124, Sweden.
出版信息
Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):678-80. doi: 10.1107/s090744499701785x.
5-Keto-4-deoxyuronate isomerase from Escherichia coli has been crystallized after partial purification. The isomerase was found to be enriched in preparations of an unrelated recombinant protein. Crystals of the isomerase were obtained from two different precipitants despite the fact that the recombinant protein represented roughly 90% of the total protein present. The crystals diffract to 2.7 A resolution and are suitable for a structure determination. The role of the isomerase in E. coli is uncertain, as E. coli is not known to degrade the polysaccharides which are potential sources of 5-keto-4-deoxyuronate.
来自大肠杆菌的5-酮基-4-脱氧uronate异构酶经过部分纯化后已结晶。发现该异构酶在一种不相关重组蛋白的制备物中得到富集。尽管重组蛋白约占总蛋白的90%，但仍从两种不同的沉淀剂中获得了异构酶晶体。这些晶体的衍射分辨率为2.7埃，适合进行结构测定。异构酶在大肠杆菌中的作用尚不确定，因为未知大肠杆菌会降解作为5-酮基-4-脱氧uronate潜在来源的多糖。
Zotero 插件